Research Topics
Genomes and GenesSpecies
| M L LudwigSummaryAffiliation: University of Michigan Country: USA Publications
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Detail Information
Publications
A new decoration for nitric oxide synthase - a Zn(Cys)4 siteM L Ludwig
Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, MI, USA
Structure 7:R73-9. 1999..A recent independent analysis of the corresponding heme domains from endothelial NOS confirms most of the features found earlier and also reveals a novel Zn(Cys)4 center - a new feature for NOS...- The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12M M Dixon
Biophysics Research Division, University of Michigan, 930 N University, Ann Arbor, MI 48109 1055, USA
Structure 4:1263-75. 1996..The structures of the AdoMet binding site and the cobalamin-binding domains (previously determined) provide a starting point for understanding the methyl transfer reactions of methionine synthase... - Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentialsD M Hoover
Biophysics Research Division and Department of Biological Chemistry, University of Michigan, 930 N Univeristy Ave, Ann Arbor, MI 48109, USA
J Mol Biol 294:725-43. 1999..The potentials and the effects of mutations in A. nidulans flavodoxin are rationalized using a thermodynamic scheme developed for C. beijerinckii flavodoxin... - Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductaseB W Lennon
Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA
Science 289:1190-4. 2000..Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees... - pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysisD L Gatti
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, USA
Biochemistry 35:567-78. 1996..Transfer of water between the chain of proton donors and the solvent also appears to be an essential part of the mechanism that provides reversible transfer of protons during the hydroxylation reaction... - Refined structures of oxidized flavodoxin from Anacystis nidulansC L Drennan
Department of Biological Chemistry and Biophysics Research Division, University of Michigan, 930 N University Ave, Ann Arbor, MI 48109, USA
J Mol Biol 294:711-24. 1999..The structures reported here provide the starting point for structure-function studies of the reduced states and of mutants, described in the accompanying paper... - Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changesM L Ludwig
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109 1055, USA
Biochemistry 36:1259-80. 1997..0 kcal/mol) and to increase the sq/hq potential by 80 mV (-1.7 kcal/mol). A thermodynamic scheme is introduced as a framework for rationalizing the properties of wild-type flavodoxin and the effects of the mutations... - Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28E E Trimmer
Department of Biological Chemistry and Biophysics Research Division, The University of Michigan, Ann Arbor, Michigan 48109 1055, USA
Biochemistry 40:6216-26. 2001..The mutant enzyme was able to bind CH(3)-H(4)folate, but reduction of the FAD cofactor was not observed. In the NADH-menadione oxidoreductase assay, the mutant demonstrated a 240-fold decrease in activity... - Interaction of flavodoxin with cobalamin-dependent methionine synthaseD A Hall
Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109 1055, USA
Biochemistry 39:10711-9. 2000..Identification of these cross-linked residues provides evidence in support of a docking model that will be useful in predicting the effects of mutations observed in mammalian homologues of E. coli flavodoxin and methionine synthase... 
A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolutionD M Hoover
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, USA
Protein Sci 6:2525-37. 1997..Structural comparisons with flavodoxins from Synechococcus PCC 7942 and Anaebaena PCC 7120 suggest other residues that may also be critical for recognition by methionine synthase...- Interaction of Escherichia coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactorD M Hoover
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109 1055, USA
Biochemistry 36:127-38. 1997..A model for the interaction of methionine synthase with flavodoxin is proposed in which flavodoxin binding leads to changes in the distribution of methionine synthase conformations... - Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]C C Correll
Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor 48109
Science 258:1604-10. 1992..0) is much higher than the potentials of plant ferredoxins. Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP(+)-reductase... - Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal siteM T Hilgers
Department of Biological Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109, USA
Proc Natl Acad Sci U S A 98:11169-74. 2001..Our analysis represents a test of structure-based functional assignment... - Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variantsM S Lah
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109
Biochemistry 33:1555-64. 1994..The functional consequences of these changes in the enzyme structure and of the introduction of the carboxyl group at 300 are described and discussed in the accompanying paper (Palfey et al., 1994b)... - Thioredoxin reductase two modes of catalysis have evolvedC H Williams
Department of Veterans Affairs Medical Center, Ann Arbor, MI, USA
Eur J Biochem 267:6110-7. 2000..P. falciparum is the major causative agent of malaria and it is hoped that the chemical difference between the two high Mr forms may be exploited for drug design... - Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactorB W Lennon
Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109, USA
Protein Sci 8:2366-79. 1999..Distributions of bending angles in published oxidized and reduced flavoenzyme structures are different from those found in studies of free flavins, indicating that the protein environment has a significant effect on bending... - The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemiaB D Guenther
Biophysics Research Division, University of Michigan, Ann Arbor 48109 1055, USA
Nat Struct Biol 6:359-65. 1999..Folate derivatives protect wild-type and mutant E. coli enzymes against flavin loss, and protect human MTHFR and the A222V mutant against thermal inactivation, suggesting a mechanism by which folate treatment reduces homocysteine levels... - Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilusM S Lah
Biophysics Research Division, University of Michigan, Ann Arbor 48109
Biochemistry 34:1646-60. 1995.... - Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymesC L Drennan
Biophysics Research Division, University of Michigan, Ann Arbor 48109 1055
Curr Opin Struct Biol 4:919-29. 1994.... - Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coliC L Luschinsky
Biophysics Research Division, University of Michigan, Ann Arbor 48109 2099
J Mol Biol 225:557-60. 1992..9 A, b = 55.4 A, c = 103.8 A. For two molecules per asymmetric unit, the calculated VM value is 2.45 A3/Da. A native data set has been collected to 3 A resolution... - Structure-based perspectives on B12-dependent enzymesM L Ludwig
Biophysics Research Division, University of Michigan, Ann Arbor 48109 1055, USA
Annu Rev Biochem 66:269-313. 1997..The intermediate radical species generated in catalysis are sequestered in the relatively hydrophilic core of an alpha/beta barrel domain of the mutase... - A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: initial characterization of seven mutant proteinsM Amaratunga
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, USA
Biochemistry 35:2453-63. 1996..These mutations asses the importance of individual residues in modulating cobalamin reactivity... - The mobile flavin of 4-OH benzoate hydroxylaseD L Gatti
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109
Science 266:110-4. 1994..Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis... - Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolutionM L Ludwig
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109
J Mol Biol 219:335-58. 1991..abstract truncated at 400 words).. - Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levelsW C Stallings
Proc Natl Acad Sci U S A 80:3884-8. 1983..Consistent with the notion of the independent evolution of the copper/zinc dismutase gene, the iron dismutase structure resembles the copper/zinc protein at neither the monomer nor the dimer level... - The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzymeJ T Jarrett
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104, USA
Biochemistry 37:12649-58. 1998..We propose a kinetic scheme for reductive methylation of wild-type cob(II)alamin enzyme by adenosylmethionine and flavodoxin hydroquinone in which slow conformational changes mask the relatively fast electron and methyl transfer steps... - Structure of oxidized flavodoxin from Anacystis nidulansW W Smith
J Mol Biol 165:737-53. 1983.... - A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilisC H Weber
Biophysics Research Division Department of Biological Chemistry University of Michigan Pathology Department University of Michigan Medical School Ann Arbor, MI 48109, USA
Structure 7:1113-24. 1999..Thus, GCT provides an excellent model for the study of catalysis by the eukaryotic cytidylyltransferases... - Manganese and iron superoxide dismutases are structural homologsW C Stallings
J Biol Chem 259:10695-9. 1984..One set of interchain contacts closely resembles the dimer interface of Fe dismutase, but the other interface utilizes an inserted polypeptide segment that has no equivalent in Fe dismutase... - The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4-A resolutionW C Stallings
J Biol Chem 260:16424-32. 1985..Only one other dimer interface occurs in the tetramer; it involves residues 55-62 and sequences near 140 and 156. The center of the oligomeric molecule is filled with solvent... - Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structuresA Carlioz
Institut Jacques Monod, Paris, France
J Biol Chem 263:1555-62. 1988....